SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P98174

- FGD1_HUMAN

UniProt

P98174 - FGD1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
FYVE, RhoGEF and PH domain-containing protein 1
Gene
FGD1, FGDY, ZFYVE3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri730 – 79061FYVE-type
Add
BLAST

GO - Molecular functioni

  1. Rho guanyl-nucleotide exchange factor activity Source: InterPro
  2. guanyl-nucleotide exchange factor activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. small GTPase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. apoptotic signaling pathway Source: Reactome
  3. cytoskeleton organization Source: UniProtKB
  4. filopodium assembly Source: UniProtKB
  5. multicellular organismal development Source: ProtInc
  6. neurotrophin TRK receptor signaling pathway Source: Reactome
  7. organ morphogenesis Source: ProtInc
  8. positive regulation of apoptotic process Source: Reactome
  9. regulation of Cdc42 GTPase activity Source: UniProtKB
  10. regulation of cell shape Source: UniProtKB
  11. regulation of small GTPase mediated signal transduction Source: Reactome
  12. signal transduction Source: ProtInc
  13. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
FYVE, RhoGEF and PH domain-containing protein 1
Alternative name(s):
Faciogenital dysplasia 1 protein
Rho/Rac guanine nucleotide exchange factor FGD1
Short name:
Rho/Rac GEF
Zinc finger FYVE domain-containing protein 3
Gene namesi
Name:FGD1
Synonyms:FGDY, ZFYVE3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:3663. FGD1.

Subcellular locationi

Cytoplasm By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Cytoplasmcytoskeleton By similarity
Note: Associated with membrane ruffles and lamellipodia By similarity.

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. lamellipodium Source: UniProtKB
  6. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Aarskog-Scott syndrome (AAS) [MIM:305400]: A rare multisystemic disorder characterized by disproportionately short stature, and by facial, skeletal and urogenital anomalies. Some patients manifest mental retardation, attention deficit disorder and hyperactivity.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051S → I in AAS. 1 Publication
VAR_019268
Natural varianti380 – 3801E → A in AAS. 1 Publication
VAR_019270
Natural varianti443 – 4431R → H in AAS. 1 Publication
VAR_019271
Natural varianti522 – 5221R → H in AAS. 1 Publication
VAR_015236
Natural varianti610 – 6101R → Q in AAS. 1 Publication
Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
VAR_015237
Defects in FGD1 are found in a patient with non-syndromal X-linked mental retardation.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi305400. phenotype.
Orphaneti915. Aarskog-Scott syndrome.
PharmGKBiPA28102.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961FYVE, RhoGEF and PH domain-containing protein 1
PRO_0000080940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei365 – 3651Phosphoserine1 Publication
Modified residuei711 – 7111Phosphothreonine1 Publication
Modified residuei715 – 7151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP98174.
PaxDbiP98174.
PRIDEiP98174.

PTM databases

PhosphoSiteiP98174.

Expressioni

Tissue specificityi

Expressed in fetal heart, brain, lung, kidney and placenta. Less expressed in liver; adult heart, brain, lung, pancreas and skeletal muscle.

Gene expression databases

BgeeiP98174.
CleanExiHS_FGD1.
GenevestigatoriP98174.

Organism-specific databases

HPAiHPA000911.

Interactioni

Subunit structurei

Interacts with DBNL/ABP1 and CTTN. May interact with CCPG1 By similarity. Binds CDC42.

Protein-protein interaction databases

BioGridi108536. 4 interactions.
MINTiMINT-2805047.
STRINGi9606.ENSP00000364277.

Structurei

3D structure databases

ProteinModelPortaliP98174.
SMRiP98174. Positions 316-786, 831-920.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini373 – 561189DH
Add
BLAST
Domaini590 – 689100PH 1
Add
BLAST
Domaini821 – 921101PH 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 18717SH3-binding Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 330324Pro-rich
Add
BLAST

Domaini

The DH domain is involved in interaction with CCPG1 By similarity.

Sequence similaritiesi

Contains 2 PH domains.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG295069.
HOGENOMiHOG000220866.
HOVERGENiHBG007506.
InParanoidiP98174.
KOiK05720.
OMAiLQMPRMP.
OrthoDBiEOG7C2R0M.
PhylomeDBiP98174.
TreeFamiTF316247.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P98174-1 [UniParc]FASTAAdd to Basket

« Hide

MHGHRAPGGA GPSEPEHPAT NPPGAAPPAC ADSDPGASEP GLLARRGSGS    50
ALGGPLDPQF VGPSDTSLGA APGHRVLPCG PSPQHHRALR FSYHLEGSQP 100
RPGLHQGNRI LVKSLSLDPG QSLEPHPEGP QRLRSDPGPP TETPSQRPSP 150
LKRAPGPKPQ VPPKPSYLQM PRMPPPLEPI PPPPSRPLPA DPRVAKGLAP 200
RAEASPSSAA VSSLIEKFER EPVIVASDRP VPGPSPGPPE PVMLPQPTSQ 250
PPVPQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV 300
SDDGPPSHSL CPGPPALASV PVALADPHRP GSQEVDSDLE EEDDEEEEEE 350
KDREIPVPLM ERQESVELTV QQKVFHIANE LLQTEKAYVS RLHLLDQVFC 400
ARLLEEARNR SSFPADVVHG IFSNICSIYC FHQQFLLPEL EKRMEEWDRY 450
PRIGDILQKL APFLKMYGEY VKNFDRAVEL VNTWTERSTQ FKVIIHEVQK 500
EEACGNLTLQ HHMLEPVQRI PRYELLLKDY LLKLPHGSPD SKDAQKSLEL 550
IATAAEHSNA AIRKMERMHK LLKVYELLGG EEDIVSPTKE LIKEGHILKL 600
SAKNGTTQDR YLILFNDRLL YCVPRLRLLG QKFSVRARID VDGMELKESS 650
NLNLPRTFLV SGKQRSLELQ ARTEEEKKDW VQAINSTLLK HEQTLETFKL 700
LNSTNREDED TPPNSPNVDL GKRAPTPIRE KEVTMCMRCQ EPFNSITKRR 750
HHCKACGHVV CGKCSEFRAR LVYDNNRSNR VCTDCYVALH GVPGSSPACS 800
QHTPQRRRSI LEKQASVAAE NSVICSFLHY MEKGGKGWHK AWFVVPENEP 850
LVLYIYGAPQ DVKAQRSLPL IGFEVGPPEA GERPDRRHVF KITQSHLSWY 900
FSPETEELQR RWMAVLGRAG RGDTFCPGPT LSEDREMEEA PVAALGATAE 950
PPESPQTRDK T 961
Length:961
Mass (Da):106,561
Last modified:February 1, 2003 - v2
Checksum:i30963F7B9931E45C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051S → I in AAS. 1 Publication
VAR_019268
Natural varianti312 – 3121P → L in non-syndromal X-linked mental retardation. 1 Publication
Corresponds to variant rs28935498 [ dbSNP | Ensembl ].
VAR_019269
Natural varianti380 – 3801E → A in AAS. 1 Publication
VAR_019270
Natural varianti443 – 4431R → H in AAS. 1 Publication
VAR_019271
Natural varianti522 – 5221R → H in AAS. 1 Publication
VAR_015236
Natural varianti610 – 6101R → Q in AAS. 1 Publication
Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
VAR_015237

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 2314AGPSE…ATNPP → RRAFGARTPGHEPA1 Publication
Add
BLAST
Sequence conflicti195 – 1951A → G in AAA57004. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11690 mRNA. Translation: AAA57004.1.
Z85987 Genomic DNA. Translation: CAI42222.1.
CH471154 Genomic DNA. Translation: EAW93179.1.
BC034530 mRNA. Translation: AAH34530.1.
CCDSiCCDS14359.1.
PIRiA55380.
RefSeqiNP_004454.2. NM_004463.2.
UniGeneiHs.709201.

Genome annotation databases

EnsembliENST00000375135; ENSP00000364277; ENSG00000102302.
GeneIDi2245.
KEGGihsa:2245.
UCSCiuc004dtg.3. human.

Polymorphism databases

DMDMi28202247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11690 mRNA. Translation: AAA57004.1 .
Z85987 Genomic DNA. Translation: CAI42222.1 .
CH471154 Genomic DNA. Translation: EAW93179.1 .
BC034530 mRNA. Translation: AAH34530.1 .
CCDSi CCDS14359.1.
PIRi A55380.
RefSeqi NP_004454.2. NM_004463.2.
UniGenei Hs.709201.

3D structure databases

ProteinModelPortali P98174.
SMRi P98174. Positions 316-786, 831-920.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108536. 4 interactions.
MINTi MINT-2805047.
STRINGi 9606.ENSP00000364277.

Chemistry

BindingDBi P98174.
ChEMBLi CHEMBL2862.

PTM databases

PhosphoSitei P98174.

Polymorphism databases

DMDMi 28202247.

Proteomic databases

MaxQBi P98174.
PaxDbi P98174.
PRIDEi P98174.

Protocols and materials databases

DNASUi 2245.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375135 ; ENSP00000364277 ; ENSG00000102302 .
GeneIDi 2245.
KEGGi hsa:2245.
UCSCi uc004dtg.3. human.

Organism-specific databases

CTDi 2245.
GeneCardsi GC0XM054488.
HGNCi HGNC:3663. FGD1.
HPAi HPA000911.
MIMi 300546. gene.
305400. phenotype.
neXtProti NX_P98174.
Orphaneti 915. Aarskog-Scott syndrome.
PharmGKBi PA28102.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295069.
HOGENOMi HOG000220866.
HOVERGENi HBG007506.
InParanoidi P98174.
KOi K05720.
OMAi LQMPRMP.
OrthoDBi EOG7C2R0M.
PhylomeDBi P98174.
TreeFami TF316247.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSi FGD1. human.
GeneWikii FGD1.
GenomeRNAii 2245.
NextBioi 9083.
PROi P98174.
SOURCEi Search...

Gene expression databases

Bgeei P98174.
CleanExi HS_FGD1.
Genevestigatori P98174.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProi IPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view ]
SMARTi SM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor."
    Pasteris N.G., Cadle A., Logie L.J., Porteous M.E.M., Schwartz C.E., Stevenson R.E., Glover T.W., Wilroy R.S., Gorski J.L.
    Cell 79:669-678(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Craniofacial.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor."
    Zheng Y., Fischer D.J., Santos M.F., Tigyi G., Pasteris N.G., Gorski J.L., Xu Y.
    J. Biol. Chem. 271:33169-33172(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-205; THR-711 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Two novel mutations confirm FGD1 is responsible for the Aarskog syndrome."
    Schwartz C.E., Gillessen-Kaesbach G., May M., Cappa M., Gorski J.L., Steindl K., Neri G.
    Eur. J. Hum. Genet. 8:869-874(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AAS HIS-522.
  10. "A mutation in the pleckstrin homology (PH) domain of the FGD1 gene in an Italian family with faciogenital dysplasia (Aarskog-Scott syndrome)."
    Orrico A., Galli L., Falciani M., Bracci M., Cavaliere M.L., Rinaldi M.M., Musacchio A., Sorrentino V.
    FEBS Lett. 478:216-220(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AAS GLN-610.
  11. "Non-syndromic X-linked mental retardation associated with a missense mutation (P312L) in the FGD1 gene."
    Lebel R.R., May M., Pouls S., Lubs H.A., Stevenson R.E., Schwartz C.E.
    Clin. Genet. 61:139-145(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NONSYNDROMAL X-LINKED MENTAL RETARDATION LEU-312.
  12. "Phenotypic and molecular characterisation of the Aarskog-Scott syndrome: a survey of the clinical variability in light of FGD1 mutation analysis in 46 patients."
    Orrico A., Galli L., Cavaliere M.L., Garavelli L., Fryns J.-P., Crushell E., Rinaldi M.M., Medeira A., Sorrentino V.
    Eur. J. Hum. Genet. 12:16-23(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AAS ILE-205; ALA-380 AND HIS-443.

Entry informationi

Entry nameiFGD1_HUMAN
AccessioniPrimary (citable) accession number: P98174
Secondary accession number(s): Q5H999, Q8N4D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 1, 2003
Last modified: September 3, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi